EFFECT OF UREY-BRADLEY-SHIMANOUCHI FORCE-FIELD ON THE HARMONIC DYNAMICS OF PROTEINS

被引：3

作者：

DERREUMAUX, P

VERGOTEN, G

机构：

[1] UNIV LILLE 2,FAC PHARM,INSERM,U279,GENIE BIOL & MED LAB,F-59045 LILLE,FRANCE

[2] UNIV LILLE 2,FAC MED,CERIM,F-59045 LILLE,FRANCE

来源：

PROTEINS-STRUCTURE FUNCTION AND GENETICS | 1991年 / 11卷 / 02期

关键词：

NORMAL MODE ANALYSIS; POTENTIAL ENERGY FUNCTION; LYS-15 AND ARG-17 RESIDUES;

D O I：

10.1002/prot.340110205

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

A normal mode analysis of bovine pancreatic trypsin inhibitor is carried out by using a Urey-Bradley-Shimanouchi potential energy function. The density of vibrational states, the magnitudes, and time scales of the atomic fluctuations are compared with experimental and theoretical results obtained by the more commonly used potential energy functions. The atomic fluctuations of Lys-15 are subject to extensive considerations as this residue is buried in the trypsin specificity pocket. It is found that Arg-17 is likely to be of importance in order to understand the way BPTI binds on trypsin.

引用

页码：120 / 132

页数：13

共 57 条

[11] A VIBRATIONAL MOLECULAR-FORCE FIELD OF MODEL COMPOUNDS WITH BIOLOGICAL INTEREST .1. HARMONIC DYNAMICS OF CRYSTALLINE UREA AT 123-K [J].